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Toxicity of Pristine and Chemically Functionalized Fullerenes to White Rot Fungus Phanerochaete chrysosporium.

ABSTRACT: Fullerenes are widely produced and applied carbon nanomaterials that require a thorough investigation into their environmental hazards and risks. In this study, we compared the toxicity of pristine fullerene (C₆₀) and carboxylated fullerene (C₆₀-COOH) to white rot fungus Phanerochaete chrysosporium. The influence of fullerene on the weight increase, fibrous structure, ultrastructure, enzyme activity, and decomposition capability of P. chrysosporium was investigated to reflect the potential toxicity of fullerene. C₆₀ did not change the fresh and dry weights of P. chrysosporium but C₆₀-COOH inhibited the weight gain at high concentrations. Both C₆₀ and C₆₀-COOH destroyed the fibrous structure of the mycelia. The ultrastructure of P. chrysosporium was changed by C₆₀-COOH. Pristine C₆₀ did not affect the enzyme activity of the P. chrysosporium culture system while C₆₀-COOH completely blocked the enzyme activity. Consequently, in the liquid culture, P. chrysosporium lost the decomposition activity at high C₆₀-COOH concentrations. The decreased capability in degrading wood was observed for P. chrysosporium exposed to C₆₀-COOH. Our results collectively indicate that chemical functionalization enhanced the toxicity of fullerene to white rot fungi and induced the loss of decomposition activity. The environmental risks of fullerene and its disturbance to the carbon cycle are discussed.

SUBMITTER: Ming Z

PROVIDER: S-EPMC5853751 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature

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Toxicity of Pristine and Chemically Functionalized Fullerenes to White Rot Fungus Phanerochaete chrysosporium.

Ming Zhu Z Feng Shicheng S Yilihamu Ailimire A Ma Qiang Q Yang Shengnan S Yang Sheng-Tao ST

Nanomaterials (Basel, Switzerland) 20180222 2

Fullerenes are widely produced and applied carbon nanomaterials that require a thorough investigation into their environmental hazards and risks. In this study, we compared the toxicity of pristine fullerene (C60) and carboxylated fullerene (C60-COOH) to white rot fungus Phanerochaete chrysosporium. The influence of fullerene on the weight increase, fibrous structure, ultrastructure, enzyme activity, and decomposition capability of P. chrysosporium was investi ...[more]

PMID: 29470407

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Project description:The activity of a self-sufficient cytochrome P450 enzyme, CYP505D6, from the lignin-degrading basidiomycete Phanerochaete chrysosporium was characterized. Recombinant CYP505D6 was produced in Escherichia coli and purified. In the presence of NADPH, CYP505D6 used a series of saturated fatty alcohols with C9-18 carbon chain lengths as the substrates. Hydroxylation occurred at the ω-1 to ω-6 positions of such substrates with C9-15 carbon chain lengths, except for 1-dodecanol, which was hydroxylated at the ω-1 to ω-7 positions. Fatty acids were also substrates of CYP505D6. Based on the sequence alignment, the corresponding amino acid of Tyr51, which is located at the entrance to the active-site pocket in CYP102A1, was Val51 in CYP505D6. To understand the diverse hydroxylation mechanism, wild-type CYP505D6 and its V51Y variant and wild-type CYP102A1 and its Y51V variant were generated, and the products of their reaction with dodecanoic acid were analyzed. Compared with wild-type CYP505D6, its V51Y variant generated few products hydroxylated at the ω-4 to ω-6 positions. The products generated by wild-type CYP102A1 were hydroxylated at the ω-1 to ω-4 positions, whereas its Y51V variant generated ω-1 to ω-7 hydroxydodecanoic acids. These observations indicated that Val51 plays an important role in determining the regiospecificity of fatty acid hydroxylation, at least that at the ω-4 to ω-6 positions. Aromatic compounds, such as naphthalene and 1-naphthol, were also hydroxylated by CYP505D6. These findings highlight a unique broad substrate spectrum of CYP505D6, rendering it an attractive candidate enzyme for the biotechnological industry.IMPORTANCEPhanerochaete chrysosporium is a white-rot fungus whose metabolism of lignin, aromatic pollutants, and lipids has been most extensively studied. This fungus harbors 154 cytochrome P450-encoding genes in the genome. As evidenced in this study, P. chrysosporium CYP505D6, a fused protein of P450 and its reductase, hydroxylates fatty alcohols (C9-15) and fatty acids (C9-15) at the ω-1 to ω-7 or ω-1 to ω-6 positions, respectively. Naphthalene and 1-naphthol were also hydroxylated, indicating that the substrate specificity of CYP505D6 is broader than those of the known fused proteins CYP102A1 and CYP505A1. The substrate versatility of CYP505D6 makes this enzyme an attractive candidate for biotechnological applications.

Dataset Information

Toxicity of Pristine and Chemically Functionalized Fullerenes to White Rot Fungus Phanerochaete chrysosporium.

Publications

Toxicity of Pristine and Chemically Functionalized Fullerenes to White Rot Fungus Phanerochaete chrysosporium.

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